Molybdopterin biosynthesis protein moeA - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P12281 (MOEA_ECOLI)

Last modified December 15, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Molybdopterin biosynthesis protein moeA

Gene names

Name:	moeA
Synonyms:	bisB, chlE, narE
Ordered Locus Names:	b0827, JW0811

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in the biosynthesis of a demolybdo-cofactor (molybdopterin), necessary for molybdo-enzymes. Seems to be involved in a step of activation of molybdenum in the form of thiomolybdenum.
Cofactor	Binds 1 magnesium ion.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homodimer. Ref.6 Ref.7
Sequence similarities	Belongs to the moeA family.

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Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	Magnesium Metal-binding
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
pfkA	P0A796	1	EBI-554393,EBI-554405

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 411

411

Molybdopterin biosynthesis protein moeA

PRO_0000170989

Secondary structure

411

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12281-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 6DBBC2B4191F5951
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FASTA

411

44,067

        10         20         30         40         50         60 
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV PGFDNSAMDG 

        70         80         90        100        110        120 
YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT GAPVPEGCEA VVMQEQTEQM 

       130        140        150        160        170        180 
DNGVRFTAEV RSGQNIRRRG EDISAGAVVF PAGTRLTTAE LPVIASLGIA EVPVIRKVRV 

       190        200        210        220        230        240 
ALFSTGDELQ LPGQPLGDGQ IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA 

       250        260        270        280        290        300 
DSQADVVISS GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN 

       310        320        330        340        350        360 
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR GVLQRNADGE 

       370        380        390        400        410 
LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE VEPFNALFGG L

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." Nohno T., Kasai Y., Saito T. J. Bacteriol. 170:4097-4102(1988) [PubMed: 3045084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Physiological and genetic analyses leading to identification of a biochemical role for the moeA (molybdate metabolism) gene product in Escherichia coli." Hasona A., Ray R.M., Shanmugam K.T. J. Bacteriol. 180:1466-1472(1998) [PubMed: 9515915] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway." Schrag J.D., Huang W., Sivaraman J., Smith C., Plamondon J., Larocque R., Matte A., Cygler M. J. Mol. Biol. 310:419-431(2001) [PubMed: 11428898] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION, SUBUNIT.
[7]	"The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin." Xiang S., Nichols J., Rajagopalan K.V., Schindelin H. Structure 9:299-310(2001) [PubMed: 11525167] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M21151 Genomic DNA. Translation: AAA23579.1.
U00096 Genomic DNA. Translation: AAC73914.1.
AP009048 Genomic DNA. Translation: BAA35515.1.

PIR

A32352.

RefSeq

AP_001458.1.
NP_415348.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FC5	X-ray	2.20	A/B	1-411	[»]
1G8L	X-ray	1.95	A/B	1-411	[»]
1G8R	X-ray	2.65	A/B	1-411	[»]
2NQK	X-ray	2.90	A/B	1-411	[»]
2NQM	X-ray	3.00	A/B	1-411	[»]
2NQN	X-ray	2.20	A/B	1-411	[»]
2NQQ	X-ray	2.40	A/B/C/D	1-411	[»]
2NQR	X-ray	2.20	A/B	1-411	[»]
2NQS	X-ray	2.50	A/B	1-411	[»]
2NQU	X-ray	2.70	A/B	1-411	[»]
2NQV	X-ray	2.82	A/B	1-411	[»]
2NRO	X-ray	2.50	A/B	1-411	[»]
2NRP	X-ray	3.00	A/B	1-411	[»]
2NRS	X-ray	2.80	A/B	1-411	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10240N.

IntAct

P12281. 9 interactions.

STRING

P12281.

Genome annotation databases

GeneID

945454.

GenomeReviews

Gene locus JW0811 in contig AP009048_GR.
Gene locus b0827 in contig U00096_GR.

KEGG

ecj:JW0811.
eco:b0827.

Organism-specific databases

EchoBASE

EB0151.

EcoGene

EG10153. moeA.

CMR

Search...

Phylogenomic databases

HOGENOM

HBG731522.

OMA

VPGFDNA.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10153-MON.
ECOL168927:B0827-MON.
MetaCyc:EG10153-MON.

Gene expression databases

Genevestigator

P12281.

Family and domain databases

InterPro

IPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_N-dom-I/II.
IPR001453. Mopterin_bd.
[Graphical view]

Gene3D

G3DSA:3.40.980.10. MPT_bd. 1 hit.

Pfam

PF00994. MoCF_biosynth. 1 hit.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]

SMART

SM00852. MoCF_biosynth. 1 hit.
[Graphical view]

PROSITE

PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

MOEA_ECOLI

Accession

Primary (citable) accession number: P12281

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	December 15, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents